9q9h

Cryo-EM structure of human Mre11-Rad50 complex bound to DNA

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

DNA repair protein RAD50

Homo sapiens

UniProt Q92878

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 4 DNA 2 Double-strand break repair protein MRE11 × 2 (P49959) DNA (50-MER) × 1 DNA (50-MER) × 1 MAGNESIUM ION × 2 ADENOSINE-5'-DIPHOSPHATE × 2 BERYLLIUM TRIFLUORIDE ION × 2 MANGANESE (II) ION × 4 water × 3 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name RAD50_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1312; UniProt 1–1312 Author chain B; PDBConstruct 1–1312; UniProt 1–1312

Double-strand break repair protein MRE11

Homo sapiens

UniProt P49959

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 4 DNA 2 DNA repair protein RAD50 × 2 (Q92878) DNA (50-MER) × 1 DNA (50-MER) × 1 MAGNESIUM ION × 2 ADENOSINE-5'-DIPHOSPHATE × 2 BERYLLIUM TRIFLUORIDE ION × 2 MANGANESE (II) ION × 4 water × 3 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name MRE11_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–708; UniProt 1–708 Author chain E; PDBConstruct 1–708; UniProt 1–708

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id9q9h
Deposition date deposition_date2025-02-26
Last revision last_revision2025-10-01
Structure title titleCryo-EM structure of human Mre11-Rad50 complex bound to DNA
Keywords keywordsMre11-Rad50-DNA complex, double-strand DNA break repair, nuclease, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

9q9h__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9q9h__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9q9h__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)44.14 Å
Rg (electron density)44.76 Å
Total Rg44.72 Å
Atom count16781
Residues1982
Excluded volume295800 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9q9h__assembly_1__model_1 hexameric (6) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (9)

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7. Citations (1)